2nvb

Contribution of Pro275 to the Thermostability of the Alcohol Dehydrogenases (ADHs)
(see also Tetrameric alcohol dehydrogenases)



Ribbon diagram of the TbADH tetramer. Monomers are colored in different colors. Pro residues (ball representation) are colored orange (Pro275) which is important for thermal stabilization and cyan (Pro100). Overlay of the structures of the wild-type holo-TbADH (colored lime, 1ykf) and the holo P275D-TbADH mutant (colored orange). Pro275 and Asp275 are labeled red. Residues within a distance of 4Å from P275D are shown (names of subunits are in brackets). Nitrogen and oxygen atoms are colored in CPK colors. Replacing Pro275 with Asp reduces the thermal stability of the enzyme: ΔT1/260min = -13.8°C, ΔT1/2CD = -18.8°C. These findings indicate that a single proline mutation is responsible for the significant differences in the thermal stability of ADHs, and show the importance of prolines in the protein stability.

About this Structure
2NVB is a Single protein structure of sequence from Thermoanaerobacter brockii. Full crystallographic information is available from OCA.

Reference
Thermal stabilization of the protozoan Entamoeba histolytica alcohol dehydrogenase by a single proline substitution., Goihberg E, Dym O, Tel-Or S, Shimon L, Frolow F, Peretz M, Burstein Y, Proteins. 2008 Feb 7;. PMID:18260103

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